2014
Therapeutic Molecules and Endogenous Ligands Regulate the Interaction between Brain Cellular Prion Protein (PrPC) and Metabotropic Glutamate Receptor 5 (mGluR5)*
Haas LT, Kostylev MA, Strittmatter SM. Therapeutic Molecules and Endogenous Ligands Regulate the Interaction between Brain Cellular Prion Protein (PrPC) and Metabotropic Glutamate Receptor 5 (mGluR5)*. Journal Of Biological Chemistry 2014, 289: 28460-28477. PMID: 25148681, PMCID: PMC4192497, DOI: 10.1074/jbc.m114.584342.Peer-Reviewed Original ResearchMeSH KeywordsAlzheimer DiseaseAmyloid beta-PeptidesAnimalsAntibodiesBinding SitesBiological AssayBrain ChemistryCell MembraneDisease Models, AnimalGene Expression RegulationHEK293 CellsHumansLigandsMiceMice, TransgenicPeptide MappingProtein BindingProtein Structure, TertiaryPrPC ProteinsReceptor, Metabotropic Glutamate 5Recombinant ProteinsSignal TransductionSmall Molecule LibrariesConceptsMetabotropic glutamate receptor 5Glutamate receptor 5Receptor 5Endogenous ligandMouse brainAD transgenic model miceCellular prion proteinAmino acids 91Transgenic model miceSoluble amyloid β (Aβ) oligomersAlzheimer's disease pathophysiologySilent allosteric modulatorsAgonists/antagonistsExtracellular AβOsMGluR5 activitySynthetic AβOsPrion proteinAmyloid-β OligomersModel miceCell membrane preparationsMGluR5Neurotoxic signalsBrain homogenatesAlzheimer's diseaseDisease pathophysiology
2013
Anatomical Plasticity of Adult Brain Is Titrated by Nogo Receptor 1
Akbik FV, Bhagat SM, Patel PR, Cafferty WB, Strittmatter SM. Anatomical Plasticity of Adult Brain Is Titrated by Nogo Receptor 1. Neuron 2013, 77: 859-866. PMID: 23473316, PMCID: PMC3594793, DOI: 10.1016/j.neuron.2012.12.027.Peer-Reviewed Original ResearchConceptsNgr1-/- miceNogo receptor 1Somatosensory cortexReceptor 1Adult cerebral cortexDendritic spine turnoverDendritic spine dynamicsAnatomical plasticityCerebral cortexControl miceSpine turnoverAxonal varicositiesWhisker removalAdult brainDendritic spinesSpine dynamicsNull miceAge 26Synaptic turnoverAnatomical connectivityConditional deletionMiceLower set pointNgR1Cortex
2007
Nogo receptor interacts with brain APP and Abeta to reduce pathologic changes in Alzheimer's transgenic mice.
Park JH, Strittmatter SM. Nogo receptor interacts with brain APP and Abeta to reduce pathologic changes in Alzheimer's transgenic mice. Current Alzheimer Research 2007, 4: 568-70. PMID: 18220524, PMCID: PMC2846284, DOI: 10.2174/156720507783018235.Peer-Reviewed Original ResearchConceptsTransgenic miceAlzheimer's diseasePlaque depositionAdult central nervous systemAlzheimer's transgenic miceNogo-66 receptorAmyloid β plaquesCentral nervous systemAxonal sproutingAβ accumulationΒ plaquesDystrophic neuritesPathologic changesNogo receptorNervous systemBrain APPDiseasePotential mechanistic basisMiceExpression increasesNGR modificationReceptorsNeurite responseNGRMechanistic basis
2006
Alzheimer Precursor Protein Interaction with the Nogo-66 Receptor Reduces Amyloid-β Plaque Deposition
Park JH, Gimbel DA, GrandPre T, Lee JK, Kim JE, Li W, Lee DH, Strittmatter SM. Alzheimer Precursor Protein Interaction with the Nogo-66 Receptor Reduces Amyloid-β Plaque Deposition. Journal Of Neuroscience 2006, 26: 1386-1395. PMID: 16452662, PMCID: PMC2846286, DOI: 10.1523/jneurosci.3291-05.2006.Peer-Reviewed Original ResearchConceptsAmyloid precursor proteinAlzheimer's diseaseAbeta levelsDystrophic neuritesPlaque depositionAmyloid-β plaque depositionCourse of ADAbeta plaque depositionTransgenic AD modelBrain Abeta levelsAD brain samplesAdult CNS axonsAxonal sprouting responseNgR expressionAbeta depositsAxonal dysfunctionPathophysiologic hypothesesSecretase processingTraumatic injuryAbeta productionDisease processAD modelBrain samplesCNS axonsPlaque deposits
2004
A Neutralizing Anti-Nogo66 Receptor Monoclonal Antibody Reverses Inhibition of Neurite Outgrowth by Central Nervous System Myelin*
Li W, Walus L, Rabacchi SA, Jirik A, Chang E, Schauer J, Zheng BH, Benedetti NJ, Liu BP, Choi E, Worley D, Silvian L, Mo W, Mullen C, Yang W, Strittmatter SM, Sah DW, Pepinsky B, Lee DH. A Neutralizing Anti-Nogo66 Receptor Monoclonal Antibody Reverses Inhibition of Neurite Outgrowth by Central Nervous System Myelin*. Journal Of Biological Chemistry 2004, 279: 43780-43788. PMID: 15297463, DOI: 10.1074/jbc.m401803200.Peer-Reviewed Original ResearchConceptsOligodendrocyte myelin glycoproteinRat dorsal root ganglion neuronsDorsal root ganglion neuronsMonoclonal antibodiesMyelin glycoproteinNeurite outgrowthMyelin proteinsUseful therapeutic approachCNS myelin substrateNogo66 receptorCentral nervous system myelinGanglion neuronsTherapeutic approachesCNS repairMyelin substrateCentral nervous system myelin proteinsInhibitory effectNgR1AntibodiesNeurite growthMyelinSystem myelinReverses inhibitionMolecular epitopes
2002
Localization of Nogo-A and Nogo-66 Receptor Proteins at Sites of Axon–Myelin and Synaptic Contact
Wang X, Chun SJ, Treloar H, Vartanian T, Greer CA, Strittmatter SM. Localization of Nogo-A and Nogo-66 Receptor Proteins at Sites of Axon–Myelin and Synaptic Contact. Journal Of Neuroscience 2002, 22: 5505-5515. PMID: 12097502, PMCID: PMC6758202, DOI: 10.1523/jneurosci.22-13-05505.2002.Peer-Reviewed Original ResearchConceptsAdult CNSLimited axonal regenerationSpinal cord injuryNogo-66 receptorInteraction of NogoAxonal plasticityCord injurySynaptic contactsAxonal regenerationNgR proteinMyelinated fibersPostnatal neuronsLocalization of NogoMyelinated axonsAxonal growthOligodendrocyte surfacePhysiologic roleAxonsNogoProtein expressionNeuronsReceptorsInhibitory proteinInjuryCNS
1990
G0 is a major growth cone protein subject to regulation by GAP-43
Strittmatter S, Valenzuela D, Kennedy T, Neer E, Fishman M. G0 is a major growth cone protein subject to regulation by GAP-43. Nature 1990, 344: 836-841. PMID: 2158629, DOI: 10.1038/344836a0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBrain ChemistryCell MembraneGAP-43 ProteinGrowth SubstancesGTP-Binding ProteinsGuanosine 5'-O-(3-Thiotriphosphate)Guanosine TriphosphateMembrane GlycoproteinsMolecular Sequence DataMolecular WeightNerve Tissue ProteinsPeptide FragmentsProtein BindingRatsReceptors, Cell SurfaceReceptors, NeurotransmitterSequence Homology, Nucleic AcidSignal TransductionThionucleotidesConceptsTransmembrane receptorsNeuronal growth cone membraneAmino-terminal domainGTP-binding proteinsGrowth cone membraneExtracellular signalsGrowth cone proteinGAP-43Cone membraneGrowth conesCone proteinNeuronal growthProteinS bindingMajor componentG0ReceptorsGTPRegulationIntracellularBindingMembraneDomain
1982
Physical separation and characterization of two types of benzodiazepine receptors.
Lo MM, Strittmatter SM, Snyder SH. Physical separation and characterization of two types of benzodiazepine receptors. Proceedings Of The National Academy Of Sciences Of The United States Of America 1982, 79: 680-684. PMID: 6281778, PMCID: PMC345810, DOI: 10.1073/pnas.79.2.680.Peer-Reviewed Original Research